ID I3U9L2_ADVKW Unreviewed; 430 AA.
AC I3U9L2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:AFK61700.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:AFK61700.1};
GN OrderedLocusNames=TKWG_06215 {ECO:0000313|EMBL:AFK61700.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK61700.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK61700.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
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DR EMBL; CP003555; AFK61700.1; -; Genomic_DNA.
DR RefSeq; WP_014749791.1; NC_017964.1.
DR AlphaFoldDB; I3U9L2; -.
DR STRING; 1036672.TKWG_06215; -.
DR KEGG; aka:TKWG_06215; -.
DR HOGENOM; CLU_015572_1_0_4; -.
DR OrthoDB; 9803027at2; -.
DR Proteomes; UP000005267; Chromosome.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR00857; pyrC_multi; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AFK61700.1}.
FT DOMAIN 232..426
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 430 AA; 45395 MW; 6CA39CF40A7914AD CRC64;
MKIVIKGGRL LDPASGTDQT GNLYIAAGRI VGMGQEPDGF ESARTIDATG KLVIPGLIDL
AVRLREPGFE HRATLESEMQ AALAGGVTSL VLPPDTEPAL DEPGLVEMLK HRARQLHQAN
LYPLGAMTNR LEGKIITEMA ELTEAGCIAF SQASLPLIDT GVLLRSMQYA KTYGYTLWLT
PLEASLSKGV AASGPFASRL GLVGVPEQAE TIALHTLFEL QKVTGTRLHI CRLSSAAGIA
LVRQAKAQGL PVTCDVSLNH LHLTDLDIGF FDSNYRLDPP LRGQRDRDAI RAGLADGTID
AVCSDHTPVD DDGKLMPFAE AEPGATGVEL LFSLVVKWAQ EEKLSLVQAL GLITTGPAAI
LKAGAPSLPG CGTLSVGAPA DIAIADADAA WTVGRDTLLS QSAHTPFVGY ELPGKIVMTL
VSGRSVWESV
//
